Mannosylglycerate synthase

Mannosylglycerate synthase
Identifiers
EC no.2.4.1.269
Databases
BRENDAenzyme data
ExPASyNiceZyme view
KEGGenzyme entry
MetaCycmetabolic pathway
Rheareactions
PDB structuresRCSB PDB PDBe PDBsum
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PMCarticles
PubMedarticles
NCBIproteins

Mannosylglycerate synthase (EC 2.4.1.269) is an enzyme with systematic name GDP-mannose:D-glycerate 2-alpha-D-mannosyltransferase.[1] It catalyses the following chemical reaction

2D representation of the chemical structure of Q27104217.
D-glyceric acid
+ GDP-mannose
 
 
 
Rightward reaction arrow with minor product(s) to top right
 
 
 
2D representation of the chemical structure of Q27098255.
2-(α-D-mannosyl)-D-glyceric acid

The enzyme characterised from transfers a mannose sugar unit from GDP-mannose to D-glyceric acid, giving 2-(α-D-mannosyl)-D-glyceric acid, with guanosine diphosphate (GDP) as a byproduct.[2][3] In thermophilic bacteria, the product protects against osmotic shock and in some cases is produced in a two-step process that uses mannosyl-3-phosphoglycerate synthase to give a phosphoglycerate intermediate which is hydrolysed by the enzyme mannosyl-3-phosphoglycerate phosphatase.[4]

References

  1. ↑ Enzyme 2.4.1.269 at KEGG Pathway Database.
  2. ↑ Martins LO, Empadinhas N, Marugg JD, Miguel C, Ferreira C, da Costa MS, Santos H (December 1999). "Biosynthesis of mannosylglycerate in the thermophilic bacterium Rhodothermus marinus. Biochemical and genetic characterization of a mannosylglycerate synthase". The Journal of Biological Chemistry. 274 (50): 35407–14. doi:10.1074/jbc.274.50.35407. PMID 10585410.
  3. ↑ Flint J, Taylor E, Yang M, Bolam DN, Tailford LE, Martinez-Fleites C, Dodson EJ, Davis BG, Gilbert HJ, Davies GJ (July 2005). "Structural dissection and high-throughput screening of mannosylglycerate synthase". Nature Structural & Molecular Biology. 12 (7): 608–14. doi:10.1038/nsmb950. PMID 15951819.
  4. ↑ Empadinhas N, Marugg JD, Borges N, Santos H, da Costa MS (2001). "Pathway for the synthesis of mannosylglycerate in the hyperthermophilic archaeon Pyrococcus horikoshii. Biochemical and genetic characterization of key enzymes". J. Biol. Chem. 276 (47): 43580–8. doi:10.1074/jbc.M108054200. hdl:10362/191445. PMID 11562374.
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